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A new method has been developed by which subunits L and M of the photosynthetic reaction centre from Rhodospirillum rubrum G-9+ can be obtained in pure form, starting form freeze-dried chromatophore membranes. The method employs extraction into a mixture of chloroform/methanol and gel permeation chromatography on a column of hydroxypropylated Sephadex G 100. Cross-contamination of the purified subunits was less than 5% (mol/mol), as estimated by manual Edman degradation. Automated Edman degradation has been carried out with both subunits in a liquid-phase sequencer. 36 amino-acid residues of subunit L and 50 residues of subunit M could be unequivocally identified. In both cases, the sequence analyses came to a premature end as the signal sudden by dropped to the level of the accidental fluctuations of the phenylthiohydantoin-derivatives background. This effect is explained by the unusual susceptibility to peptide bond cleavage of certain threonine residues which probably underwent N leads to O acyl shift during the cleavage reactions. The N-terminal sequences have been compared to those of subunits L and M of the photosynthetic reactions centre from Rhodopseudomonas sphaeroides R-26 (sutton, M.R., Rosen, D., Feher, G. &amp; Steiner, L.A. (1982) Biochemistry 21, 3842-3849). The homology among subunits L is close to 90% and thus markedly higher than that among subunits M (32%). This finding indicates a pre-eminent role of subunit L in the primary events of photosynthetic energy conversion.

hoppe-seyler's zeitschrift für physiologische chemie

N-Terminal Sequences of Subunits L and M of the Photosynthetic Reaction Centre from  Rhodospirillum rubrum  G-9 + . Separation of the Subunits by Gel Filtration on Hydroxypropylated Sephadex G 100 in Organic Solvents